dbPTM

DIAC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DIAC_HUMAN
UniProt AC	Q01459
Protein Name	Di-N-acetylchitobiase
Gene Name	CTBS
Organism	Homo sapiens (Human).
Sequence Length	385
Subcellular Localization	Lysosome.
Protein Description	Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase..
Protein Sequence	MSRPQLRRWRLVSSPPSGVPGLALLALLALLALRLAAGTDCPCPEPELCRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTVATFGKYDSELMCYAHSKGARVVLKGDVSLKDIIDPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRCYNYTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPWYGYDYTCLNLSEDHVCTIAKVPFRGAPCSDAAGRQVPYKTIMKQINSSISGNLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMWNANCLDYSGDAVAKQQTEEMWEVLKPKLLQR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	LRRWRLVSSPPSGVP HHCEECCCCCCCCCH	41.54	-
174	Phosphorylation	FHREIEGSQVTFDVA HHHHCCCCEEEEEEE	14.53	24114839
177	Phosphorylation	EIEGSQVTFDVAWSP HCCCCEEEEEEECCC	13.38	24114839
183	Phosphorylation	VTFDVAWSPKNIDRR EEEEEECCCCCCCCC	19.09	24719451
193	N-linked_Glycosylation	NIDRRCYNYTGIADA CCCCCCCCCCCHHHH	31.36	UniProtKB CARBOHYD
228	N-linked_Glycosylation	AAANAPYNQTLTGYN HHCCCCCCCCCCCCC	27.57	UniProtKB CARBOHYD
262	N-linked_Glycosylation	GYDYTCLNLSEDHVC CCCEEECCCCCCCEE	43.60	UniProtKB CARBOHYD
282	Phosphorylation	PFRGAPCSDAAGRQV CCCCCCCCCCCCCCC	29.26	25219547
291	Phosphorylation	AAGRQVPYKTIMKQI CCCCCCCHHHHHHHH	23.16	25219547
293	Phosphorylation	GRQVPYKTIMKQINS CCCCCHHHHHHHHHH	22.06	25219547
299	N-linked_Glycosylation	KTIMKQINSSISGNL HHHHHHHHHHCCCCC	27.49	16399764
299	N-linked_Glycosylation	KTIMKQINSSISGNL HHHHHHHHHHCCCCC	27.49	16399764
335	Phosphorylation	VWYDNPQSISLKATY ECCCCCCCEEEEEEE	18.53	24719451
337	Phosphorylation	YDNPQSISLKATYIQ CCCCCCEEEEEEEEE	29.12	24719451
361	Phosphorylation	WNANCLDYSGDAVAK EECCCCCCCCCHHHH	11.12	-
362	Phosphorylation	NANCLDYSGDAVAKQ ECCCCCCCCCHHHHH	29.84	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of DIAC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DIAC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DIAC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DIAC_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DIAC_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299, AND MASSSPECTROMETRY.	19159218 [Abstract]